Processivity of DNA polymerases: two mechanisms, one goal

Z Kelman; J Hurwitz; M O'Donnell

doi:10.1016/s0969-2126(98)00014-8

Processivity of DNA polymerases: two mechanisms, one goal

Structure. 1998 Feb 15;6(2):121-5. doi: 10.1016/s0969-2126(98)00014-8.

Authors

Z Kelman¹, J Hurwitz, M O'Donnell

Affiliation

¹ Department of Molecular Biology, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA. z-kelman@ski.mskcc.org

PMID: 9519403
DOI: 10.1016/s0969-2126(98)00014-8

Abstract

Replicative DNA polymerases are highly processive enzymes that polymerize thousands of nucleotides without dissociating from the DNA template. The recently determined structure of the Escherichia coli bacteriophage T7 DNA polymerase suggests a unique mechanism that underlies processivity, and this mechanism may generalize to other replicative polymerases.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

MeSH terms

Bacteriophage T4 / enzymology
Bacteriophage T7 / enzymology
DNA Replication / physiology*
DNA-Directed DNA Polymerase / chemistry*
DNA-Directed DNA Polymerase / metabolism
Models, Molecular
Protein Conformation

Substances

DNA replicase
bacteriophage T7 induced DNA polymerase
DNA-Directed DNA Polymerase

Abstract

Publication types

MeSH terms

Substances

Grants and funding